ID I3JWG1_ORENI Unreviewed; 410 AA.
AC I3JWG1;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Zona pellucida sperm-binding protein 3 {ECO:0000256|ARBA:ARBA00017980, ECO:0000256|RuleBase:RU367066};
GN Name=LOC102077631 {ECO:0000313|Ensembl:ENSONIP00000013206.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000013206.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000013206.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Component of the zona pellucida, an extracellular matrix
CC surrounding oocytes which mediates sperm binding, induction of the
CC acrosome reaction and prevents post-fertilization polyspermy. The zona
CC pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4.
CC ZP3 is essential for sperm binding and zona matrix formation.
CC {ECO:0000256|RuleBase:RU367066}.
CC -!- SUBCELLULAR LOCATION: Zona pellucida {ECO:0000256|RuleBase:RU367066}.
CC Cell membrane {ECO:0000256|RuleBase:RU367066}; Single-pass type I
CC membrane protein {ECO:0000256|RuleBase:RU367066}.
CC -!- DOMAIN: The ZP domain is involved in the polymerization of the ZP
CC proteins to form the zona pellucida. {ECO:0000256|RuleBase:RU367066}.
CC -!- PTM: Proteolytically cleaved before the transmembrane segment to yield
CC the secreted ectodomain incorporated in the zona pellucida.
CC {ECO:0000256|RuleBase:RU367066}.
CC -!- SIMILARITY: Belongs to the ZP domain family. ZPC subfamily.
CC {ECO:0000256|ARBA:ARBA00006735, ECO:0000256|RuleBase:RU367066}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_005474482.1; XM_005474425.3.
DR AlphaFoldDB; I3JWG1; -.
DR Ensembl; ENSONIT00000013216.2; ENSONIP00000013206.2; ENSONIG00000010507.2.
DR GeneID; 102077631; -.
DR KEGG; onl:102077631; -.
DR eggNOG; ENOG502QSZF; Eukaryota.
DR GeneTree; ENSGT01030000234567; -.
DR HOGENOM; CLU_047091_2_0_1; -.
DR InParanoid; I3JWG1; -.
DR OMA; GMIYISC; -.
DR OrthoDB; 4268616at2759; -.
DR TreeFam; TF331369; -.
DR Proteomes; UP000005207; Linkage group LG14.
DR GO; GO:0035805; C:egg coat; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0035804; F:structural constituent of egg coat; IEA:UniProtKB-UniRule.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IEA:UniProtKB-UniRule.
DR GO; GO:0035803; P:egg coat formation; IEA:UniProtKB-UniRule.
DR GO; GO:2000344; P:positive regulation of acrosome reaction; IEA:UniProtKB-UniRule.
DR Gene3D; 2.60.40.4100; Zona pellucida, ZP-C domain; 1.
DR Gene3D; 2.60.40.3210; Zona pellucida, ZP-N domain; 1.
DR InterPro; IPR042235; ZP-C.
DR InterPro; IPR048290; ZP_chr.
DR InterPro; IPR001507; ZP_dom.
DR InterPro; IPR017977; ZP_dom_CS.
DR PANTHER; PTHR11576; ZONA PELLUCIDA SPERM-BINDING PROTEIN 3; 1.
DR PANTHER; PTHR11576:SF2; ZONA PELLUCIDA SPERM-BINDING PROTEIN 3; 1.
DR Pfam; PF00100; Zona_pellucida; 1.
DR PRINTS; PR00023; ZPELLUCIDA.
DR SMART; SM00241; ZP; 1.
DR PROSITE; PS00682; ZP_1; 1.
DR PROSITE; PS51034; ZP_2; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU367066};
KW Cleavage on pair of basic residues {ECO:0000256|RuleBase:RU367066};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|RuleBase:RU367066};
KW Extracellular matrix {ECO:0000256|RuleBase:RU367066};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU367066};
KW Signal {ECO:0000256|RuleBase:RU367066}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|RuleBase:RU367066"
FT CHAIN 22..410
FT /note="Zona pellucida sperm-binding protein 3"
FT /evidence="ECO:0000256|RuleBase:RU367066"
FT /id="PRO_5025707255"
FT DOMAIN 110..364
FT /note="ZP"
FT /evidence="ECO:0000259|PROSITE:PS51034"
FT REGION 38..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 410 AA; 45427 MW; 14E3A70048809584 CRC64;
MGSRQLVVFS FVLAWVRLSD ARFHSLNVPT HLGIKAQRPA VTEADAPGEP DRVHSSQSTQ
QAAKLQSKQN QQALEPLSWK FPEDPVVQVN KPPLKFELKQ PVAAYRVAVR CGESKIFVEV
SRDFLGLGKL IKPEEISLGG CSATEIDDSS HVLVFESELH SCGSKLVLTE NAFIYAFALV
YNPKVFGRSG ITRSQSAVIR LECRYQRQHS ASSHPEPPAW MSSEANRQAQ TQQHLSLKLM
TDDWKFERTS NRYALVDVIH MEAAVLLQTL TPLRVLVDSC VATTNSDFTS GQREALINDG
CLGGQHTISR FMPRSQPDKL RLQVAVHSLG LQGMIYISCL LKAISASAPV TIENKACSFY
EGMWMAIDGK NEFCTCCEST CGMRKIRALS DNATAERWEA EVTVGPIVVE
//
